Physical and functional interactions between herpes simplex virus immediate-early proteins ICP4 and ICP27

摘要: The ordered expression of herpes simplex virus type 1 (HSV-1) genes, during the course a productive infection, requires action immediate-early regulatory proteins. Using protein interaction assay, we demonstrate specific in vitro protein-protein interactions between ICP4 and ICP27, two proteins HSV-1 that are essential for replication. We map multiple points contact these Furthermore, by coimmunoprecipitation experiments, following. (i) ICP4-ICP27 complexes present extracts from infected cells. (ii) ICP27 binds preferentially to less modified forms ICP4, is extensively posttranslationally. also demonstrate, performing electrophoretic mobility shift assays supershifts with monoclonal antibodies or both DNA-protein complex noncanonical binding site HSV thymidine kinase (TK) gene. cells ICP27-deficient viruses, impaired its ability form TK but not canonical alpha4 However, able probe, absence when overproduced mammalian expressed bacteria. These data suggest inability cell bind probe does reflect requirement physical presence complex. Rather, they imply likely modulate DNA activity affecting posttranslational modification status. Therefore, propose addition established role as posttranscriptional regulator gene expression, may transcription either through direct indirect regions, ICP4.